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Related Concept Videos

Antibody Structure and Classes01:25

Antibody Structure and Classes

Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
Antibody Structure01:10

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Antibody Structure01:10

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Transcytosis of IgG01:15

Transcytosis of IgG

Transcytosis is the process in which molecules are internalized by endocytosis, transported across the cell, and released through exocytosis from the opposite end of the cell. Molecules such as insulin, immunoglobulins, and certain nutrients are transferred through the recycling endosomes by recycling and transcytosis.
IgG molecules from a mother undergo transcytosis starting around 13 weeks of gestation. The amount of IgG transferred and entering the fetal blood circulation increases with...
Diversity of Antigen Receptors01:28

Diversity of Antigen Receptors

Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
Before encountering any antigen, lymphocytes express these receptors. On B cells, the antigen receptor is a membrane-bound antibody molecule called BCR; on T cells, it is a T cell receptor or TCR. B and T cell receptors are composed of two...

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Updated: May 9, 2026

Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing
08:51

Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing

Published on: March 15, 2019

Global structures of IgG isotypes expressing identical variable regions.

Ertan Eryilmaz1, Alena Janda, Jungwook Kim

  • 1Department of Biochemistry, The Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.

Molecular Immunology
|August 6, 2013
PubMed
Summary

Murine immunoglobulin G (IgG) structures show isotype-dependent domain orientations in solution. Structural differences in the constant (C) region influence the variable (V) region, impacting antibody specificity and affinity.

Keywords:
AntigenConstant domainImmunoglobulinIsotypeSAXSVariable domainX-ray crystallography

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Last Updated: May 9, 2026

Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing
08:51

Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing

Published on: March 15, 2019

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Area of Science:

  • Immunology
  • Structural Biology
  • Biochemistry

Background:

  • Immunoglobulin (Ig) molecules were traditionally viewed as having independent variable (V) and constant (C) regions.
  • Recent findings indicate C regions induce allosteric changes in V regions, affecting antibody specificity and affinity.

Purpose of the Study:

  • To investigate the cross-domain interrelationship within murine IgG isotypes.
  • To explore how local C region structures influence V region conformation and antibody function.

Main Methods:

  • Solution small-angle X-ray scattering (SAXS) was used to analyze four V region-identical murine IgG isotypes.
  • X-ray crystallography determined the high-resolution structure of the IgG3 Fab fragment.

Main Results:

  • SAXS revealed distinct, isotype-dependent Y-shaped structures in solution for the IgG isotypes.
  • The IgG3 Fab crystal structure exhibited significant differences compared to a related IgG1 Fab structure.
  • IgG3 displayed unique solution behavior, including aggregate formation, suggesting enhanced avidity through polyvalent complexes.

Conclusions:

  • Murine IgG V and C domains structurally influence each other.
  • The V region's structure significantly impacts the overall Ig structure.
  • Observed structural variations may explain isotype-related differences in antigen specificity for antibodies with identical V regions.